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Literature summary extracted from

  • Chen, C.; Beck, B.W.; Krause, K.; Pettitt, B.M.
    Solvent participation in Serratia marcescens endonuclease complexes (2006), Proteins, 62, 982-995.
    View publication on PubMed

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.30.2 Mg2+ molecular dynamic simulations, interaction with enzyme monomer-DNA complex via 6 ligands, which are changing during the reaction simulation, e.g. Asn119 loses its coordination while Glu127 becomes a ligand, overview Serratia marcescens

Organism

EC Number Organism UniProt Comment Textmining
3.1.30.2 Serratia marcescens
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
3.1.30.2 endonucleolytic cleavage to 5'-phosphomononucleotide and 5'-phosphooligonucleotide end-products catalytic mechanism, enzyme monomer-DNA binding complex, hydration sites and influence of solvent on structure and reaction, active site structure Serratia marcescens
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.30.2 additional information the subunits of the dimer function independently as monomers, molecular dynamic simulations involving Mg2+, modelling of complex building with DNA Serratia marcescens ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.30.2 dimer monomer and dimer of the enzyme are catalytically active Serratia marcescens
3.1.30.2 monomer monomer and dimer of the enzyme are catalytically active Serratia marcescens
3.1.30.2 More the subunits of the dimer function independently as monomers, molecular dynamic simulations, modelling of complex building with DNA, hydration sites of the enzyme depending on solvent density, overview Serratia marcescens

Synonyms

EC Number Synonyms Comment Organism
3.1.30.2 Serratia marcescens endonuclease
-
 Serratia marcescens
3.1.30.2 SMnase
-
 Serratia marcescens